SGD Paper 
Ozdemir A, et al. (2005) Characterization of Lysine 56 of Histone H3 as an Acetylation Site in Saccharomyces cerevisiae. J Biol Chem 280(28):25949-52
Abstract: Post-translational histone modifications abound and regulate multiple nuclear processes. Most modifications are targeted to the amino-terminal domains of histones. Here we report the identification and characterization of acetylation of lysine 56 within the core domain of histone H3. In the crystal structure of the nucleosome, lysine 56 contacts DNA. Phenotypic analysis suggests that lysine 56 is critical for histone function and that it modulates formamide resistance, ultraviolet radiation sensitivity and sensitivity to hydroxyurea. We show that the acetylated form of H3-K56 is present during interphase, metaphase and S-phase. Finally, reverse genetic analysis indicates that none of the known histone acetyl transferases is solely responsible for H3-K56 acetylation in Saccharomyces cerevisiae.
| Status: Published | Type: Journal Article | PubMed ID: 15888442 |
Topics addressed in this paper
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